Research workbench
AlphaFold monomer V2.0 prediction for retinoic acid receptor rxr- alpha-a (A2T929)
Analyse AlphaFold monomer V2.0 prediction for retinoic acid receptor rxr- alpha-a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2T929
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Retinoic acid receptor rxr-alpha-a
- UniProt
- A2T929
- Pockets
- 3 · best druggability 0.83
Structure
1 distinct chain · 43% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoic acid receptor rxr-alpha-a | protein | 430 | 43% helix, 3% strand | A2T929 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.83 | 0.96 | 30 | empty |
| 2 | 131 | 0.39 | 0.74 | 21 | empty |
| 3 | 69 | 0.31 | 0.74 | 16 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A2T929
- Elsewhere: UniProt A2T929 · AlphaFold DB A2T929
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